2iad: Difference between revisions

Revision as of 11:33, 28 July 2008

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File:2iad.png

Template:STRUCTURE 2iad

CLASS II MHC I-AD IN COMPLEX WITH AN INFLUENZA HEMAGGLUTININ PEPTIDE 126-138CLASS II MHC I-AD IN COMPLEX WITH AN INFLUENZA HEMAGGLUTININ PEPTIDE 126-138

Template:ABSTRACT PUBMED 9529149

About this StructureAbout this Structure

2IAD is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues., Scott CA, Peterson PA, Teyton L, Wilson IA, Immunity. 1998 Mar;8(3):319-29. PMID:9529149

Page seeded by OCA on Mon Jul 28 11:33:52 2008

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-'''CLASS II MHC I-AD IN COMPLEX WITH AN INFLUENZA HEMAGGLUTININ PEPTIDE 126-138'''
+===CLASS II MHC I-AD IN COMPLEX WITH AN INFLUENZA HEMAGGLUTININ PEPTIDE 126-138===
-==Overview==
+<!--
-We have determined the structures of I-Ad covalently linked to an ovalbumin peptide (OVA323-339) and to an influenza virus hemagglutinin peptide (HA126-138). The floor of the peptide-binding groove contains an unusual beta bulge, not seen in I-E and DR structures, that affects numerous interactions between the alpha and beta chains and bound peptide. Unlike other MHC-peptide complexes, the peptides do not insert any large anchor residues into the binding pockets of the shallow I-Ad binding groove. The previously identified six-residue "core" binding motif of I-Ad occupies only the P4 to P9 pockets, implying that specificity of T cell receptor recognition of I-Ad-peptide complexes can be accomplished by peptides that only partially fill the MHC groove.
+The line below this paragraph, {{ABSTRACT_PUBMED_9529149}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9529149 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9529149}}
 ==About this Structure==
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